BMRB Entry 18588

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18588

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Title:
Backbone 1H, 15N, 13C Assignments of the N-terminal Part of Tyrosine tRNA Synthase from Bacillus stearothermophilus
Deposition date:
2012-07-10
Original release date:
2012-10-18
Authors:
Krejcirikova, Anna; Tugarinov, Vitali
Citation:

Citation: Krejcirikova, Anna; Tugarinov, Vitali. "3D-TROSY-based backbone and ILV-methyl resonance assignments of a 319-residue homodimer from a single protein sample."  J. Biomol. NMR 54, 135-143 (2012).
PubMed: 22960997

Assembly members:

Assembly members:
Tyr_tRNA_Synthase, polymer, 327 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Bacillus stearothermophilus   Taxonomy ID: 1422   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus stearothermophilus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: Pet15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Tyr_tRNA_Synthase: MDLLAELQWRGLVNQTTDED GLRKLLNEERVTLYCGFDPT ADSLHIGHLATILTMRRFQQ AGHRPIALVGGATGLIGDPS GKKSERTLNAKETVEAWSAR IKEQLGRFLDFEADGNPAKI KNNYDWIGPLDVITFLRDVG KHFSVNYMMAKESVQSRIET GISFTEFSYMMLQAYDFLRL YETEGCRLQIGGSDQWGNIT AGLELIRKTKGEARAFGLTI PLVTKADGTKFGKTESGTIW LDKEKTSPYEFYQFWINTDD RDVIRYLKYFTFLSKEEIEA LEQELREAPEKRAAQKTLAE EVTKLVHGEEALRQAIRISL EHHHHHH

Data sets:
Data typeCount
13C chemical shifts900
15N chemical shifts299
1H chemical shifts299

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tyr_tRNA_Synthase1

Entities:

Entity 1, Tyr_tRNA_Synthase 327 residues - Formula weight is not available

1   METASPLEULEUALAGLULEUGLNTRPARG
2   GLYLEUVALASNGLNTHRTHRASPGLUASP
3   GLYLEUARGLYSLEULEUASNGLUGLUARG
4   VALTHRLEUTYRCYSGLYPHEASPPROTHR
5   ALAASPSERLEUHISILEGLYHISLEUALA
6   THRILELEUTHRMETARGARGPHEGLNGLN
7   ALAGLYHISARGPROILEALALEUVALGLY
8   GLYALATHRGLYLEUILEGLYASPPROSER
9   GLYLYSLYSSERGLUARGTHRLEUASNALA
10   LYSGLUTHRVALGLUALATRPSERALAARG
11   ILELYSGLUGLNLEUGLYARGPHELEUASP
12   PHEGLUALAASPGLYASNPROALALYSILE
13   LYSASNASNTYRASPTRPILEGLYPROLEU
14   ASPVALILETHRPHELEUARGASPVALGLY
15   LYSHISPHESERVALASNTYRMETMETALA
16   LYSGLUSERVALGLNSERARGILEGLUTHR
17   GLYILESERPHETHRGLUPHESERTYRMET
18   METLEUGLNALATYRASPPHELEUARGLEU
19   TYRGLUTHRGLUGLYCYSARGLEUGLNILE
20   GLYGLYSERASPGLNTRPGLYASNILETHR
21   ALAGLYLEUGLULEUILEARGLYSTHRLYS
22   GLYGLUALAARGALAPHEGLYLEUTHRILE
23   PROLEUVALTHRLYSALAASPGLYTHRLYS
24   PHEGLYLYSTHRGLUSERGLYTHRILETRP
25   LEUASPLYSGLULYSTHRSERPROTYRGLU
26   PHETYRGLNPHETRPILEASNTHRASPASP
27   ARGASPVALILEARGTYRLEULYSTYRPHE
28   THRPHELEUSERLYSGLUGLUILEGLUALA
29   LEUGLUGLNGLULEUARGGLUALAPROGLU
30   LYSARGALAALAGLNLYSTHRLEUALAGLU
31   GLUVALTHRLYSLEUVALHISGLYGLUGLU
32   ALALEUARGGLNALAILEARGILESERLEU
33   GLUHISHISHISHISHISHIS

Samples:

sample_1: Tyr tRNA Synthase, [U-13C; U-15N; U-2H], 0.8 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAD77088 GAD11882 GAJ57796
GB AAA22877 ADI25737 AEV20456 AGE23390 AKM20083
REF WP_011232277 WP_013144460 WP_015375638 WP_020278069 WP_033014498
SP P00952 P04077 Q5KW48
AlphaFold P00952 P04077 Q5KW48

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks